Dislocation and Degradation of Proteins from the Endoplasmic Reticulum (Current Topics in Microbiology and Immunology Book 300)

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Management number 232107342 Release Date 2026/06/18 List Price US$42.64 Model Number 232107342
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The present volume of Current Topics in Microbiology and Immunology c- tains seven chapters that illuminate various aspects of a protein’s genesis and terminal fate in the endoplasmic reticulum (ER). This area is of immediate medical relevance and has blossomed, to no small extent, because of the study of molecules central to the function of the immune system [immunogl- ulins, T cell receptors, major histocompatibility complex (MHC)-encoded products]. Similarly, the clever strategies used by bacteria or viruses to gain a foothold in the host and ensure their continued survival have uncovered altogether new cell biological principles. It is therefore ?tting that a special volume be devoted to the interplay between pathways of protein degradation in the ER and a wide variety of pathogens. The concept of quality control emerged with the appreciation that, in the case of multimeric glycoproteins, any unpaired glycoprotein subunit had great dif?culties leaving its site of synthesis—the ER—and was destroyed instead. Free immunoglobulin heavy chains were probably the earliest documented example of this kind, and were long known to cause pathology when their accumulation went unchecked. Increased knowledge of the biosynthetic pathways of glycoproteins allowed the identi?cation of the ER as an important site where such quality control decisions were made. The T cell receptor for antigen, long considered the paradigm of this mode of degradation, led the way in these early explorations. Read more

ASIN B001GMAHCC
XRay Not Enabled
ISBN13 978-3540280071
Edition 2005th
Language English
File size 2.2 MB
Page Flip Not Enabled
Publisher Springer
Word Wise Not Enabled
Print length 185 pages
Accessibility Learn more
Part of series Current Topics in Microbiology and Immunology
Publication date February 4, 2006
Enhanced typesetting Not Enabled

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